BRENDA - Enzyme Database
show all sequences of 3.4.23.29

Crystal structure of aspartic proteinase from Irpex lacteus in complex with inhibitor pepstatin

Fujimoto, Z.; Fujii, Y.; Kaneko, S.; Kobayashi, H.; Mizuno, H.; J. Mol. Biol. 341, 1227-1235 (2004)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
purified enzyme in complex with inhibitor pepstatin, hanging drop vapour diffusion method, 0.005 ml of 10 mg/ml protein is mixed with 0.005 ml of reservoir solution containing 50% ammonium sulfate in 10 mM sodium citrate-sulfate buffer, pH 5.4, 20°C, X-ray diffraction structure determination and analysis at 1.3 A resolution, structure modeling
Irpex lacteus
Inhibitors
Inhibitors
Commentary
Organism
Structure
pepstatin
binding structure
Irpex lacteus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Irpex lacteus
-
formerly Irpex lacteus
-
Reaction
Reaction
Commentary
Organism
Milk clotting activity, broad specificity, but fails to cleave Leu15-Tyr or Tyr16-Leu of insulin B chain
catalytic mechanism, transition state model, substrate binding structure and mechanism
Irpex lacteus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the enzyme requires hydrophobic amino acids at P1 and/or P1' positions and at P3 and/or P4 positions, the enzyme shows high milk-clotting activity
669833
Irpex lacteus
?
-
-
-
-
Crystallization (Commentary) (protein specific)
Crystallization
Organism
purified enzyme in complex with inhibitor pepstatin, hanging drop vapour diffusion method, 0.005 ml of 10 mg/ml protein is mixed with 0.005 ml of reservoir solution containing 50% ammonium sulfate in 10 mM sodium citrate-sulfate buffer, pH 5.4, 20°C, X-ray diffraction structure determination and analysis at 1.3 A resolution, structure modeling
Irpex lacteus
Inhibitors (protein specific)
Inhibitors
Commentary
Organism
Structure
pepstatin
binding structure
Irpex lacteus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
additional information
the enzyme requires hydrophobic amino acids at P1 and/or P1' positions and at P3 and/or P4 positions, the enzyme shows high milk-clotting activity
669833
Irpex lacteus
?
-
-
-
-
Other publictions for EC 3.4.23.29
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
668788
Kobayashi
-
Polyporopepsin ...
Irpex lacteus
Handbook of Proteolytic Enzymes (Barrett, J. ; Rawlings, N. D. ; Woessner, J. F. , eds. )
1
113-115
2004
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1
1
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2
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1
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6
1
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1
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1
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669833
Fujimoto
Crystal structure of aspartic ...
Irpex lacteus
J. Mol. Biol.
341
1227-1235
2004
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30729
Kobayashi
-
Cloning and sequence analysis ...
Irpex lacteus
Agric. Biol. Chem.
53
1927-1933
1989
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1
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30730
Kobayashi
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Purification and characterizat ...
Irpex lacteus
Agric. Biol. Chem.
49
2393-2397
1985
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6
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1
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11
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2
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1
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6
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11
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2
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2
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1
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30728
Kobayashi
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Substrate specificity of a car ...
Irpex lacteus
Agric. Biol. Chem.
47
1921-1923
1983
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3
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1
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1
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1
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30731
Kawai
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Studies on the milk-clotting e ...
Irpex lacteus
Agric. Biol. Chem.
40
1463-1469
1976
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